Prolamine solution to block pancreatic duct.
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Alcoholism↗
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Chromosomal location of genes coding for endosperm proteins of Hordeum chilense, determined by two-dimensional electrophoresis of wheat-H. chilense chromosome addition lines.
The proteins of Hordeum chilense grain were resolved into 25 major components by two-dimensional electrophoresis. Their solubilities in aqueous alcohol solutions were determined to distinguish prolamin storage proteins from metabolic and structural proteins. The prolamins were divided into two groups, based on the presence or absence of intermolecular disulfide bonds determined by gel-filtration chromatography. Using an incomplete set of Chinese Spring wheat-H. chilense disomic addition lines, the structural genes of 21 of the 26 most dominant seed proteins were assigned to chromosomes. The great majority of the prolamin genes, including those coding for a high molecular weight (HMW) prolamin subunit, was present on chromosome 1 Hch. However, a small number of prolamin genes also occurred on chromosomes 5 Hch and 7 Hch. A minor protein, probably belonging to the nonstorage group of proteins, is coded by genes on 5 Hch. Various ditelosomic addition lines and ditelosomic and disomic substitution lines for chromosome 7 Hch were also analyzed by electrophoresis. This technique revealed that the genes for three major prolamins occur on the beta arm of chromosome 7 Hch and that a gene for a minor protein, also thought to be a prolamin, occurs on the alpha arm. These results are discussed in relation to the evolution of prolamin genes in the Triticeae.
Chromosome Mapping↗
Identification of a cytoskeleton-associated 120 kDa RNA-binding protein in developing rice seeds.
During rice seed development, prolamine RNAs are localized to the surface of the prolamine storage protein bodies (PBs), organelles bounded by the endoplasmic reticulum (ER). The exact mechanism by which prolamine RNAs are enriched on this ER subdomain is not known but recent evidence indicates the directed transport and targeting of prolamine RNAs to the prolamine PBs. As such a process involves RNA signal determinants and cytoskeleton-interacting proteins that recognize these signals, we obtained an enriched cytoskeleton-PB fraction and identified a prominent RNA-binding activity, Rp120, by RNA-binding UV-cross-linking assay. Recombinant cDNA clones of Rp120 revealed that the primary sequence shared considerable structural homology to the human transcriptional coactivator p100 and possessed a modular organization, four nucleic acid-binding SN domains, a tudor domain and a coil-coil domain. Consistent with the presence of SN domains, Rp120 binds a variety of RNAs including prolamine RNA. Interaction with the latter RNA, however, was specific as binding activity was evident only to the prolamine 3' UTR and not to the 5' UTR or coding sequences. Rp120 is also able to interact with other proteins as its sedimentation behavior in sucrose density gradient suggests an association with the cytoskeleton. The presence of a tudor domain, suggested to have a role in RNA processing or transport, together with the SN and coiled-coil domains are consistent with the view that Rp120 may be involved in RNA sorting in rice endosperm.
Amino Acid Sequence↗
[Screening and genetic analysis of rice glutelin mutant].
The contribution of rice as a protein source is important. Rice seed protein can be divided into four forms, glutelin (57 kDa, 37-39 kDa, 22-23 kDa), prolamine (13 kDa), albumin (16 kDa) and globulin (10 kDa, 26 kDa) on its solubility. Glutelin is the major storage protein of rice and accounted for 80% of total protein found in the rice grain, the mature glutelin comprises an acidic (37-39 kDa) and an basic subunit (22-23 kDa) coming from a common precursor (57 kDa) by post-transcriptional hydrolytic cleavage. Prolamine is the second important. Rice seed proteins localize in two types of protein bodies, PB-I, PB-II. PB-I containing prolamine is indigestible, whereas PB-II being rich in glutelin is digestible. The nutritional value of rice could thus be raised by improving its digestible protein glutelin content. On the other hand, the character of low digestible protein is also an important target of rice breeding. Low protein rice is required for the diet of patients with kidney disease. Three glutelin mutants, W3660, W204, W379, were found by screening 168 rice varieties through SDS-PAGE analysis of the seeds total proteins. The amounts of 37-39 kDa and 22-23 kDa glutelin subunits were much lower and that of 13 kDa prolamine polypeptide was higher in W3660 seeds than in ordinary rice; The amounts of 37-39 kDa and 22-23 kDa glutelin subunits in W204 or W379 seeds were between those in W3660 and ordinary rice. Especially, in W379 seed, there was a large quantity of 57 kDa polypeptide. For characterizing the genetics of the glutelin mutant, the cross population between W3660 and Otorokimochi was constructed. SDS-PAGE analysis of the progeny seed total proteins showed, low glutelin content was always accompanied by high prolamine content; all F1 seeds had low glutelin and high prolamine content; the segregation of low glutelin and normal type in F2 seeds was 3:1; the genotypes of F2 plants were deduced by the analysis of F3 seeds, and among F2 plants the ratio of homozygotes of low glutelin, heterozygotes of low glutelin and homozygotes of normal type was about 1:2:1. These results proved that the trait of low glutelin and high prolamine was controlled by a single dominant gene and could be inherited by its progeny.
Glutens↗
Wheat starch, gliadin, and the gluten-free diet.
Individuals with celiac disease generally are advised to follow a lifelong gluten-free diet and avoid consumption of the prolamins gliadin (wheat), secalin (rye), and hordein (barley). Although the designation of the diet as glutenfree may imply that the diet contains zero gluten, this is not necessarily true. In some countries (eg, United States, Canada), the gluten-free diet is completely devoid of gluten and is based on foods such as rice and corn that are naturally gluten free. In others (eg, Scandinavia, United Kingdom), the gluten-free diet may include foods such as wheat starch that have been rendered gluten free but nonetheless contain small amounts of toxic prolamins. The discrepancy in the use of foods rendered gluten free exists because the amount of toxic prolamins that individuals with celiac disease may consume without damaging the mucosa of the small intestine is unknown. Minimal research has been conducted on the toxicity of foods rendered gluten free, and there are no definitive data about whether the small amount of prolamin found in these products is safe to consume. Nonetheless, the Codex Alimentarius Standard for gluten-free foods allows a certain amount of prolamin in foods designated gluten free, and these products have been used in many countries for several decades. Well-designed, scientifically sound studies are needed to help determine the amount of toxic prolamins, if any, that may be safely consumed by individuals with celiac disease. Until this research is conducted, dietitians in the United States should continue to advise their patients against the use of wheat starch and other foods rendered gluten free.
Celiac Disease↗
The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase.
Rice (Oryza sativa) accumulates prolamins and glutelins as storage proteins. The latter storage protein is synthesized on the endoplasmic reticulum (ER) as a 57-kD proglutelin precursor, which is then processed into acidic and basic subunits in the protein storage vacuole. Three esp2 mutants, CM1787, EM44, and EM747, contain larger amounts of the 57-kD polypeptide and corresponding lower levels of acidic and basic glutelin subunits than normal. Electron microscopic observation revealed that esp2 contained normal-appearing glutelin-containing protein bodies (PB-II), but lacked the normal prolamin-containing PB (PB-I). Instead, numerous small ER-derived PBs of uniform size (0.5 microm in diameter) and low electron density were readily observed. Immunoblot analysis of purified subcellular fractions and immunocytochemistry at the electron microscopy level showed that these new PBs contained the 57-kD proglutelin precursor and prolamin polypeptides. The 57-kD proglutelin was extracted with 1% (v/v) lactic acid solution only after removal of cysteine-rich prolamin polypeptides, suggesting that these proteins form glutelin-prolamin aggregates via interchain disulfide bonds within the ER lumen. The endosperm of esp2 mutants contains the lumenal chaperones, binding protein and calnexin, but lacks protein disulfide isomerase (PDI) at the protein and RNA levels. The transcript of PDI was expressed in the seed only during the early stage of seed development in the wild type. These results suggest that PDI plays an essential role in the segregation of proglutelin and prolamin polypeptides within the ER lumen.
Blotting, Northern↗
Amino acid compositions of different protein fractions in developing grains of NP 113 barley and its high lysine Notch-2 mutant.
The percent distributions of protein fractions namely albumin + globulin, prolamine and glutelin were studied in developing grains of NP 113 barley and its high lysine mutant Notch-2. During development the percentage of albumin + globulin fraction decreased in NP 113, while those of prolamine and glutelin remained unchanged. The increase in prolamine was substantial from 24 to 31DAA. In Notch-2 the trend followed by albumin + globulin and prolamine was like that in NP 113, while the glutelin fraction showed an increase as compared to 10 DAA. The percent of albumin + globulin was slightly higher in Notch-2 as compared to NP 113. The absolute amount (mg/grain) of all the protein fractions increased during development in both NP 113 and its mutant Notch-2. During the grain development the prolamine content was substantially lower in the mutant than in the parent NP 113. The albumin + globulin content per endosperm was in general also higher in NP 113 than Notch-2. Amino acid analysis of the protein fractions did not reveal significant changes in lysine between NP 113 and Notch-2. Thus, the improvement in lysine in the mutant is primarily due to reduced synthesis of the prolamine fraction and not due to an increase in lysine in the mutant hordein fraction. Part of the improvement in lysine may also be due to increase in the percentage of albumin + globulin fractions which is lysine rich.
Amino Acids↗
Messenger RNA targeting of rice seed storage proteins to specific ER subdomains.
Rice seeds, a rich reserve of starch and protein, are a major food source in many countries. Unlike the seeds of other plants, which typically accumulate one major type of storage protein, rice seeds use two major classes, prolamines and globulin-like glutelins. Both storage proteins are synthesized on the endoplasmic reticulum (ER) and translocated to the ER lumen, but are then sorted into separate intracellular compartments. Prolamines are retained in the ER lumen as protein bodies whereas glutelins are transported and stored in protein storage vacuoles. Mechanisms responsible for the retention of prolamines within the ER lumen and their assembly into intracisternal inclusion granules are unknown, but the involvement of RNA localization has been suggested. Here we show that the storage protein RNAs are localized to distinct ER membranes and that prolamine RNAs are targeted to the prolamine protein bodies by a mechanism based on RNA signal(s), a process that also requires a translation initiation codon. Our results indicate that the ER may be composed of subdomains that specialize in the synthesis of proteins directed to different compartments of the plant endomembrane system.
3' Untranslated Regions↗
Polypeptide compositions and NH2-terminal amino acid sequences of proteins in foxtail and proso millets.
Seed protein of foxtail and proso millets were fractionated into polypeptides that were analyzed for their major protein, prolamin, and the NH2-terminal amino acid sequences of the proteins were determined. The proteins extracted from foxtail and proso millets were 64.1% and 80.0% prolamin, respectively. The polypeptides of the prolamins were classified into two groups. The major polypeptides of 27-19 kDa were rich in leucine and alanine, whereas the 17-14 kDa polypeptides were rich in methionine and cysteine. Glutelin-like proteins that were extracted with a reducing reagent were high in proline content, the major polypeptides being 17 and 20 kDa. The NH2-terminal amino acid sequence showed that the major polypeptides of prolamin were homologous to alpha-zein and a glutelin-like protein containing the Pro-Pro-Pro sequence, like the repetitive sequence of gamma-zein. Although the prolamin consisted of a similar subunit to that of zein, polypeptides with various pI values were found among them.
Amino Acid Sequence↗
Nucleotide sequence of a B1 hordein gene and the identification of possible upstream regulatory elements in endosperm storage protein genes from barley, wheat and maize.
The B-hordeins are the major group of prolamin storage proteins in barley (Hordeum vulgare L.) and they are encoded by a small multigene family that is expressed specifically in the developing endosperm. We report the complete nucleotide sequence of a clone of one B-hordein gene (pBHR184). The cloned gene contains no introns and belongs to the B1 sub-family of B-hordein genes. Comparison of the 5'-flanking sequences of pBHR184 with those of related S-rich prolamin genes from wheat shows that several short sequences within 600 bp upstream of the translation initiation codon are strongly conserved. A sequence that is conserved at around -300 bp in the S-rich prolamins is also conserved at similar locations in genes encoding the two major classes of maize prolamin (the Z19 and Z21 zeins) and appears to be unique to prolamin genes. We discuss the possible role of this '-300 element' in the control of gene expression in the developing cereal endosperm.
Amino Acid Sequence↗
A monoclonal antibody that recognizes a potential coeliac-toxic repetitive pentapeptide epitope in gliadins.
OBJECTIVES: Antibodies that detect coeliac-toxic prolamins from wheat, barley and rye are important tools for controlling the diet of coeliac disease patients. Recently, a monoclonal antibody R5 that recognizes wheat gliadin, barley hordein and rye secalin equally was described. In this study, the epitope recognized by R5 was investigated. METHODS: Both a phage-displayed heptapeptide library and overlapping peptides spanning the sequence of alpha- and gamma-type gliadins (pepscan) were screened for binding of R5. RESULTS: Both techniques yielded comparable pentapeptide consensus sequences (phage display QXPW/FP; pepscan QQPFP). According to recent observations, this peptide stretch may be of key importance in the pathogenicity of coeliac disease. This sequence occurs repetitively in prolamins (in gamma- and omega-type prolamins more frequently than in alpha-type prolamins) together with several homologous peptide stretches, which are recognized less strongly. CONCLUSIONS: R5 seems to be a good candidate for the specific detection of putative coeliac disease-active sequences in prolamins and thus represents a valuable tool for the quality control of gluten-free food.
Amino Acid Sequence↗
Proteomics characterization of different bran proteins between aromatic and nonaromatic rice (Oryza sativa L. ssp. indica).
Proteomic approach is applied for the analysis of seed brans of 14 rice varieties (Oryza sativa L. ssp. indica) which can classify to five aromatic rice and nine nonaromatic rice. The two-dimensional electrophoresis (2-DE) protein patterns for 14 rice varieties were similar within pH ranges of 3-10 and 4-7. To characterize aromatic group-specific proteins, we compared 2-D gels of aromatic rice to nonaromatic rice using PDQUEST image analysis. Four out of six differential spots were identified as hypothetical proteins, but one (SSP 7003) was identified by matrix assisted laser desoption/ionization-quardrupole-time of fight (MALDI-Q-TOF) as prolamin with three matching peptides based on NCBI database. Prolamin is a class of storage proteins with three different polypeptides of 10, 13, and 16 kDa. Spot SSP7003 was identified as a 13 kDa polypeptide of prolamin by combination of mass spectroscopy and N-terminal sequence analyses. In contrast, one sulfur-rich 16 kDa polypeptide of prolamin was found in extremely high intensity in brans of deep-water rice compared to nondeep-water rice. Our results suggest that proteomics is a powerful step to open the way for the identification of rice varieties.
2-Propanol↗
Enzyme-linked immunosorbent assay for quantitation of cereal proteins toxic in coeliac disease.
Coeliac disease is revealed by polypeptides in the prolamin fraction of wheat, barley, rye and oats. Recovery depends on adherence to a strict cereal-free diet. A few methods for quantitation of the wheat prolamin, gliadin, have been described. In order to assess the suitability of food products for inclusion in the coeliac diet an assay should measure the total amount of potentially toxic cereal proteins. An inhibition ELISA was developed, by use of a purified, polyclonal prolamin-antibody, reacting with gliadin and gliadin-like polypeptides. The antibody did not react with maize, millet, rice or soya prolamins. The assay had a detection limit of 1 ng antigen with a very high degree of accuracy. The interassay coefficient of variation including the day-to-day variation, was close to 30%, which is acceptable for the clinical applications of the assay. The flour of buckwheat was analyzed for antigen content. An amount of 39.5 micrograms gliadin-like polypeptides/g flour was measured, which corresponds to 0.06% of the gliadin content in wheat flour.
Celiac Disease↗
An analysis of cereals that react with serum antibodies in patients with coeliac disease.
Sera from six children with active coeliac disease, and elevated titres against gliadins and from six age-matched controls, were examined for IgG antibodies against different cereal proteins by a solid-phase radioimmunoassay. Antibodies to the major wheat proteins and the prolamines of other cereals were present in low titre in all control sera. In coeliac sera, significantly higher titres were found against A-gliadin, as well as against hexaploid and tetraploid wheat whole gliadins. Gliadin peptic-tryptic digest retained a significant antigenic activity, completely lost by peptic-tryptic-pancreatic digest. High titres were also found when coeliac sera were tested against wheat glutenins, albumins, and globulins, as well as against barley, oats, and maize prolamines; rice prolamines gave lower titres. Serum from whole gliadins and A-gliadin immunized rabbits showed a similar spectrum of reactivity against prolamines as coeliac sera. Our results indicate a dissociation between immunogenic properties of cereal proteins and toxicity in coeliac disease.
Antibodies↗
Naturally developing antibodies to wheat gliadin fractions and to other cereal antigens in rabbits, rats and guinea pigs on normal laboratory diets.
Rabbits, rats and guinea pigs on normal laboratory diets were examined for gliadin and other cereal antibodies comparable to those found in the sera of human coeliac patients. Many of the rabbits had very high levels of gliadin antibodies. Rats showed much lower titres more comparable to the findings in normal human sera. In both these species the reactivity was directed principally against the alpha-gliadins. The spectrum of reactivity against the prolamines of other cereals was again comparable to that of human coeliac sera. A difference, however, was the high reactivity with maize prolamine; this was decidedly lower in sera of coeliac patients. Guinea pigs were distinctive in having relatively no serum antibodies to wheat gliadin and also minimal reactivity to the albumins, globulins and glutenins of wheat. Normal guinea pigs did, however, have antibodies to oat and maize prolamines. Following parenteral injection with total ethanol-soluble wheat gliadin, guinea pigs developed high-titred antibodies, not only to wheat gliadin fractions 1-8 (alpha-, beta-, gamma- and omega-gliadins), but also to all the cereal prolamines except those of rice. These investigations are steps in the evaluation of the role of circulating gliadin antibodies in gluten-sensitive enteropathy.
Animals↗
Sequence analysis of 22 kDa-like alpha-coixin genes and their comparison with homologous zein and kafirin genes reveals highly conserved protein structure and regulatory elements.
Several genomic and cDNA clones encoding the 22 kDa-like alpha-coixin, the alpha-prolamin of Coix seeds, were isolated and sequenced. Three contiguous 22 kDa-like alpha-coixin genes designated alpha-3A, alpha-3B and alpha-3C were found in the 15 kb alpha-3 genomic clone. The alpha-3A and alpha-3C genes presented in-frame stop codons at position +652. The two genes with truncated ORFs are flanking the alpha-3B gene, suggesting that the three alpha-coixin genes may have arisen by tandem duplication and that the stop codon was introduced before the duplication. Comparison of the deduced amino acid sequences of alpha-coixin clones with the published sequences of 22 kDa alpha-zein and 22 kDa-like alpha-kafirin revealed a highly conserved protein structure. The protein consists of an N-terminus, containing the signal peptide, followed by ten highly conserved tandem repeats of 15-20 amino acids flanked by polyglutamines, and a short C-terminus. The difference between the 22 kDa-like alpha-prolamins and the 19 kDa alpha-zein lies in the fact that the 19 kDa protein is exactly one repeat motif shorter than the 22 kDa proteins. Several putative regulatory sequences common to the zein and kafirin genes were identified within both the 5' and 3' flanking regions of alpha-3B. Nucleotide sequences that match the consensus TATA, CATC and the ca. -300 prolamin box are present at conserved positions in alpha-3B relative to zein and kafirin genes. Two putative Opaque-2 boxes are present in alpha-3B that occupies approximately the same positions as those identified for the 22 kDa alpha-zein and alpha-kafirin genes. Southern hybridization, using a fragment of a maize Opaque-2 cDNA clone as a probe, confirmed the presence of Opaque-2 homologous sequences in the Coix and sorghum genomes. The overall results suggest that the structural and regulatory genes involved in the expression of the 22 kDa-like alpha-prolamin genes of Coix, sorghum and maize, originated from a common ancestor, and that variations were introduced in the structural and regulatory sequences after species separation.
Amino Acid Sequence↗
Measurement of gluten using a monoclonal antibody to a sequenced peptide of alpha-gliadin from the coeliac-activating domain I.
A monoclonal antibody, raised against a sequenced 54 amino-acid peptide from the coeliac-activating N-terminal region of alpha-gliadin, was used in an assay for the measurement of gluten in foods. A double-sandwich ELISA using a polyclonal capture antibody produced standard curves for unfractionated gliadin and its alpha, beta, gamma and omega subfractions, and for rye, barley and oat prolamins. The sensitivity of the assay for unfractionated gliadin and rye prolamins was 15 ng/ml, for barley and oat prolamins 125 and 250 ng/ml, respectively. Prolamins from coeliac non-toxic rice, maize, millet and sorghum did not cross-react in the assay.
Antibodies, Monoclonal↗
Gliadin as a stimulator of innate responses in celiac disease.
In celiac disease (CD) we have the prototype of an immune mediated response dominated by the activation of the adaptive immune system and in particular of CD4+ HLA class II restricted T cells. Various seminal studies have established the precise mechanism of how antigen (prolamine) specific activation of CD4+ mucosal T cells occurs. Thus, CD is a condition in which T cells and their activation is the essential hinge in the pathogenic process. These functional studies have provided the explanation for the genetic association between CD and certain HLA alleles (HLA DQ2 and DQ8). These genetic, molecular and functional studies have permitted the clarification of a powerful Th1 dominated pro-inflammatory response that characterises the small intestine of active CD patients. Despite this unassailable set of information and reports there are some intriguing points that have been raised by a series of studies which have indicated that CD is not only defined by an aberrant prolamine-induced activation of the adaptive immune system. New evidence and re-assessments of old studies, point to a more complex pathogenic cascade, which may help to unravel some of the residual obscure points of CD pathogenesis. Here, we outline the current concepts that indicate a direct involvement of the adaptive immune system and we discuss all the evidence supporting a direct activation of the innate immune system by fragments of prolamines, which are not recognized T cell epitopes and how they could influence CD. The gliadin-induced activation of the 'innate' immune system might also have a significant role in the induction and persistence of many CD complications and most definitively for the most aggressive one, namely mucosal T cell lymphomas. We further suggest a novel way to harness the unwanted immune response to toxic prolamine, and thus indicate new potential therapeutic strategies to treat or at least control CD.
Animals↗